多位点蛋白质修饰中的动力学滞后现象
Dynamical hysteresis in multisite protein modification
摘要：
多位点蛋白质修饰是细胞控制蛋白质功能的普遍机制。我们最近提出了一个多位点蛋白质修饰的动力学描述，它体现了该过程的所有基本特征（E。Milotti，A.德尔法布罗角Dalla Pellegrina和R. Chignola，Physica A，in press），我们已经使用这个模型来分析这个机制的稳定性和时间尺度。相同的模型可以用来理解系统如何响应刺激：在这里，我们表明，它显示频率依赖的动态滞后。这种行为与在磁系统中观察到的行为密切相似，但存在一些差异。通过选择跨越已知生物学范围的模型参数，我们发现频率依赖性特征覆盖了所观察到的分子细胞内信号振荡的频带，这表明这种机制可能在细胞信息处理中起重要作用。
英文摘要：
Multisite protein modification is a ubiquitous mechanism utilized by cells to control protein functions. We have recently proposed a dynamical description of multisite protein modification which embodies all the essential features of the process (E. Milotti, A. Del Fabbro, C. Dalla Pellegrina, and R. Chignola, Physica A, in press), and we have used this model to analyze the stability and the time-scales of this mechanism. The same model can be used to understand how the system responds to stimuli: here we show that it displays frequency-dependent dynamical hysteresis. This behavior closely parallels -- with the due differences -- what is observed in magnetic systems. By selecting model parameters that span the known biological ranges, we find that the frequency-dependent features cover the band of the observed oscillations of molecular intracellular signals, and this suggests that this mechanism may have an important role in cellular information processing.
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